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An analysis of methyltransferase SsoII-DNA contacts in the enzyme-substrate complexстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Vorob’eva O.V., Kariagina A.S., Volkov E.M., Viriasov M.B., Oretskaya T.S., Kubareva E.A.
- Журнал: Russian Journal of Bioorganic Chemistry
- Том: 28
- Номер: 5
- Год издания: 2002
- Издательство: Maik Nauka/Interperiodica Publishing
- Местоположение издательства: Russian Federation
- Первая страница: 363
- Последняя страница: 370
- DOI: 10.1023/A:1020463810179
- Аннотация: The functional groups of the DNA methylation site that are involved in the DNA interaction with methyltransferase SsoII at the recognition stage were identified. The contacts in the enzyme-substrate complex were analyzed in the presence of S-adenosyl-L-homocysteine using the interference footprinting assay with formic acid, hydrazine, dimethyl sulfate, or N-ethyl-N-nitrosourea as a modifying reagent. It was shown that the replacement of the central A.T by the G.C pair in the methylation site did not affect the enzyme-DNA interaction, whereas the use of a substrate with one chain methylated (monomethylated substrate) instead of the unmethylated substrate dramatically changes the DNA contacts. The binding constants of unmethylated and monomethylated substrates with methyltransferase SsoII in the presence of S-adenosyl-L-homocysteine were calculated.
- Добавил в систему: Карягина-Жулина Анна Станиславовна